Catalytic domains of tyrosine kinases determine the phosphorylation sites within c-Cbl.
Article Details
- CitationCopy to clipboard
Grossmann AH, Kolibaba KS, Willis SG, Corbin AS, Langdon WS, Deininger MW, Druker BJ
Catalytic domains of tyrosine kinases determine the phosphorylation sites within c-Cbl.
FEBS Lett. 2004 Nov 19;577(3):555-62.
- PubMed ID
- 15556646 [ View in PubMed]
- Abstract
Catalytic (SH1) domains of protein tyrosine kinases (PTKs) demonstrate specificity for peptide substrates. Whether SH1 domains differentiate between tyrosines in a physiological substrate has not been confirmed. Using purified proteins, we studied the ability of Syk, Fyn, and Abl to differentiate between tyrosines in a common PTK substrate, c-Cbl. We found that each kinase produced a distinct pattern of c-Cbl phosphorylation, which altered the phosphotyrosine-dependent interactions between c-Cbl and CrkL or phosphatidylinositol 3'-kinase (PI3-K). Our data support the concept that SH1 domains determine the final sites of phosphorylation once PTKs reach their target proteins.